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Aspartokinase Homoserine Dehydrogenase
Hierarchy: | ∟ ∟ ∟ ∟ Aspartokinase Homoserine Dehydrogenase 23 coordinate concepts∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ Aspartokinase Homoserine Dehydrogenase 23 coordinate concepts∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ Aspartokinase Homoserine Dehydrogenase 23 coordinate concepts∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ Aspartokinase Homoserine Dehydrogenase 23 coordinate concepts∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ ∟ |
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History note: | Alcohol Oxidoreductases (1973-1975) | Aspartic Acid (1973-1975) | Homoserine (1973-1975) | Multienzyme Complexes (1973-1975) | Phosphotransferases, ATP (1974-1975)X |
historyNote*: | 91(76); was see under MULTIENZYME COMPLEXES 1976-90
X |
publicMeSHNote*: | 91; was see under MULTIENZYME COMPLEXES 1976-90
X |
Scope note: | An enzyme complex consisting of aspartokinase, EC 2.7.2.4, and homoserine dehydrogenase, EC 1.1.1.3. The complex has been isolated from E. coli and consists of four identical subunits with a molecular weight of 85,000. The enzyme complex is involved in the biosynthesis of amino acids of the aspartate family.
X |
activeMeSHYear*: | |
dateCreated*: | 1975-07-23X |
dateEstablished*: | 1991-01-01X |
dateRevised*: | 2003-07-09X |
recordAuthorizer*: | sjnX |
recordMaintainer*: | ssbX |
recordOriginator*: | RLSX |
Type: | |
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Labels and equivalent concepts: | Aspartokinaasihomoseriinidehydrogenaasi (fi) XAspartoquinasa Homoserina Deshidrogenasa (es) κινάση ασπαρτικού-δεϋδρογονάση ομοσερίνης (el) Aspartokinase-Homoserin-Dehydrogenase (de) dehydrogenasa aspartokinasy homoserinu (cs) Aspartocinasa Homoserina Deshidrogenasa (es, replaced) |
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